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tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
mechanism
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tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
ordered mechanism
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tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
ordered bi bi mechanism
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tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
ordered bi bi mechanism
tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
detailed mechanism
tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
kinetic analysis
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tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
kinetic analysis
tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
interactions between enzyme and acyl-CoA and peptide substrates, formation of a high affinity reaction intermediate
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tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
peptide binding site
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tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
peptide binding site
tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
active site
tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
myristoyl-CoA binding site
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tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
myristoyl-CoA binding site
tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
requires alanine at position 5 of substrate peptides
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tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
binding of myristoyl-CoA to the enzyme occurs through at least a 2-step process, X-ray data structure analysis of a binary complex between enzyme and inhibitor S-(2-oxo)-pentadecyl-CoA and ternary with peptide substrate
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tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
binding of myristoyl-CoA to the enzyme occurs through at least a 2-step process, X-ray data structure analysis of a binary complex between enzyme and inhibitor S-(2-oxo)-pentadecyl-CoA and ternary with peptide substrate
tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
binding of myristoyl-CoA to the enzyme occurs through at least a 2-step process, X-ray data structure analysis of a binary complex between enzyme and inhibitor S-(2-oxo)-pentadecyl-CoA and ternary with peptide substrate
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tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
Glu290, Val-291 and His293 within conserved region EEVEH, are essential for catalysis
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tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
PEST regions for recognition by clapains, putative regulatory enzymes
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tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
cooperativity between acyl-CoA and peptide binding sites
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tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
The enzyme from yeast is highly specific for tetradecanoyl-CoA, and highly specific for N-terminal glycine in oligopeptides containing serine in the 5-position. The enzyme from mammalian heart transfers acyl groups to a specific 51 kDa acceptor protein
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tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
myristoylation by NMT proceeds via an ordered bi-bi reaction mechanism in which binding of myristoyl-CoA generates a second binding pocket for the docking of the substrate protein. The myristate group from myristoyl-CoA is then transferred to the N-terminal glycine of the bound protein in a nucleophilic addition-elimination reaction. This is followed by stepwise release, first of the free CoA and then the N-myristoylated protein
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tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
myristoylation by NMT proceeds via an ordered bi-bi reaction mechanism in which binding of myristoyl-CoA generates a second binding pocket for the docking of the substrate protein. The myristate group from myristoyl-CoA is then transferred to the N-terminal glycine of the bound protein in a nucleophilic addition-elimination reaction. This is followed by stepwise release, first of the free CoA and then the N-myristoylated protein
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tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
myristoylation by NMT proceeds via an ordered bi-bi reaction mechanism in which binding of myristoyl-CoA generates a second binding pocket for the docking of the substrate protein. The myristate group from myristoyl-CoA is then transferred to the N-terminal glycine of the bound protein in a nucleophilic addition-elimination reaction. This is followed by stepwise release, first of the free CoA and then the N-myristoylated protein
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tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
myristoylation by NMT proceeds via an ordered bi-bi reaction mechanism in which binding of myristoyl-CoA generates a second binding pocket for the docking of the substrate protein. The myristate group from myristoyl-CoA is then transferred to the N-terminal glycine of the bound protein in a nucleophilic addition-elimination reaction. This is followed by stepwise release, first of the free CoA and then the N-myristoylated protein
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tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
myristoylation by NMT proceeds via an ordered bi-bi reaction mechanism in which binding of myristoyl-CoA generates a second binding pocket for the docking of the substrate protein. The myristate group from myristoyl-CoA is then transferred to the N-terminal glycine of the bound protein in a nucleophilic addition-elimination reaction. This is followed by stepwise release, first of the free CoA and then the N-myristoylated protein
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tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
myristoylation by NMT proceeds via an ordered bi-bi reaction mechanism in which binding of myristoyl-CoA generates a second binding pocket for the docking of the substrate protein. The myristate group from myristoyl-CoA is then transferred to the N-terminal glycine of the bound protein in a nucleophilic addition-elimination reaction. This is followed by stepwise release, first of the free CoA and then the N-myristoylated protein
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tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
myristoylation by NMT proceeds via an ordered bi-bi reaction mechanism in which binding of myristoyl-CoA generates a second binding pocket for the docking of the substrate protein. The myristate group from myristoyl-CoA is then transferred to the N-terminal glycine of the bound protein in a nucleophilic addition-elimination reaction. This is followed by stepwise release, first of the free CoA and then the N-myristoylated protein
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tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
N-myristoylation follows an ordered bi bi reaction mechanism in which myristoyl-CoA first binds to the NMT molecule inducing a conformational change and thus allowing for substrate binding followed by a direct nucleophilic addition-elimination reaction and the sequential release of CoA and the myristoyl-peptide
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tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
N-myristoylation follows an ordered bi bi reaction mechanism in which myristoyl-CoA first binds to the NMT molecule inducing a conformational change and thus allowing for substrate binding followed by a direct nucleophilic addition-elimination reaction and the sequential release of CoA and the myristoyl-peptide
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tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
N-myristoylation follows an ordered bi bi reaction mechanism in which myristoyl-CoA first binds to the NMT molecule inducing a conformational change and thus allowing for substrate binding followed by a direct nucleophilic addition-elimination reaction and the sequential release of CoA and the myristoyl-peptide
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